2izx: Difference between revisions

==Overview==

Localization of cyclic AMP (cAMP)-dependent protein kinase (PKA) by A, kinase-anchoring proteins (AKAPs) restricts the action of this broad, specificity kinase. The high-resolution crystal structures of the docking, and dimerization (D/D) domain of the RIIalpha regulatory subunit of PKA, both in the apo state and in complex with the high-affinity anchoring, peptide AKAP-IS explain the molecular basis for AKAP-regulatory subunit, recognition. AKAP-IS folds into an amphipathic alpha helix that engages an, essentially preformed shallow groove on the surface of the RII dimer D/D, domains. Conserved AKAP aliphatic residues dominate interactions to RII at, the predominantly hydrophobic interface, whereas polar residues are, important in conferring R subunit isoform specificity. Using a peptide, screening approach, we have developed SuperAKAP-IS, a peptide that is, 10,000-fold more selective for the RII isoform relative to RI and can be, used to assess the impact of PKA isoform-selective anchoring on, cAMP-responsive events inside cells.

==About this Structure==

[[Category: pka]]